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Fish and Shellfish Immunology Fish & Shellfish Immunology 32 (2012) 598e608 Contents lists available at SciVerse ScienceDirect Fish & Shellfish Immunology journal homepage: www.elsevier.com/locate/fsi Short communication Molecular characterization of three L-type lectin genes from channel catfish, Ictalurus punctatus and their responses to Edwardsiella ictaluri challenge Hao Zhang a,b, Eric Peatman a, Hong Liu a, Tingting Feng a, Liqiao Chen b, Zhanjiang Liu a,* a The Fish Molecular Genetics and Biotechnology Laboratory, Department of Fisheries and Allied Aquacultures and Program of Cell and Molecular Biosciences, Aquatic Genomics Unit, Auburn University, 203 Swingle Hall, Auburn, AL 36849, USA b School of Life Science, East China Normal University, Shanghai 200062, China article info abstract Article history: L-type lectins have a leguminous lectin domain and can bind to high-mannose type oligosaccharides. In Received 22 November 2011 the secretory pathway, L-type lectins play crucial roles in selective protein trafficking, sorting and tar- Received in revised form geting. Three L-type lectins were cloned in the channel catfish, Ictalurus punctatus, the 53 kDa endo- 22 December 2011 plasmic reticulum ER-Golgi intermediate compartment protein (ERGIC-53), the vesicular integral protein Accepted 23 December 2011 of 36 kDa (VIP36) and VIP36-like. Phylogenetic analysis indicated that the catfish genes are orthologous Available online 6 January 2012 to their counterparts in other species. Southern blot analysis demonstrated that all three L-type lectin genes are likely single-copy genes in the catfish genome. Analysis of expression in healthy tissues using Keywords: Lectin quantitative real time RT-PCR indicated that all three genes are expressed widely in all tested tissues, but Immune response with strong tissue preference of expression: ERGIC-53 was found to be abundantly expressed in the liver, Catfish VIP36 was found to be abundantly expressed in the head-kidney, whereas VIP36-like was found to be ERGIC-53 abundantly expressed in the brain. Upon infection with Edwardsiella ictaluri, expressions of the three VIP36 genes all had significant up-regulation in the head-kidney, but had distinct expression patterns: ERGIC- 53 was gradually induced with the highest expression 7 days after challenge in the head-kidney, but was down-regulated in the liver, spleen, and brain. VIP36 was highly induced in the head-kidney, and 3 days after challenge in the brain, but was not up-regulated in any other tissues or timepoints after challenge. Expression levels of the catfish VIP36-like gene appeared to also respond to infection, albeit with differing patterns among the tested tissues. Taken together, our results indicate that all three L-type lectin genes may be involved in the immune responses of catfish after infection with E. ictaluri. Ó 2011 Elsevier Ltd. All rights reserved. 1. Introduction Drosophila [2].InCaenorhabditis elegans, ERGIC-53 can affect the transport of yet other glycoproteins [2]. Recent studies have shown L-type lectins, including the 53 kDa endoplasmic reticulum that mutation in human ERGIC-53 results in combined deficiency of (ER)-Golgi intermediate compartment protein ERGIC-53 [1] and factor V and factor VIII, causing an autosomal recessive bleeding VIP36 [2], are intracellular lectins that are located in luminal disorder characterized by coordinated reduction of both clotting compartments of the secretary pathway and function in the traf- proteins [4,6,7]. ficking, sorting and targeting of maturing glycoproteins [3]. ERGIC- The 36 kDa vesicular integral protein (VIP36) is a type I 53 genes in many species are annotated as lectin, mannose-binding membrane glycoprotein with a CRD similar to that of ERGIC-53, and 1 (LMAN1) while VIP36 genes are annotated as lectin, mannose- which is thought to act as a cargo receptor for glycoprotein quality binding 2 (LMAN2). ERGIC-53 is a mannose-specific lectin that control in the Golgi [8,9]. VIP36 has specificity for high-mannose cycles between the ER and the ER-Golgi intermediate compartment type glycans of the Man6e9 but its efficient binding requires the (ERGIC) [4]. It has been shown that ERGIC-53 is a cargo transport additional presence of an a-substituted asparagine residue [2,5], receptor for some glycoproteins in ER export [2,5]. ERGIC-53 may and the binding of VIP36 to high-mannose type glycans is inde- þ affect b-integrin traffic, as demonstrated by a mutant of ERGIC-53 pendent of Ca2 [2,10]. Knock-down of VIP36-like mRNA using that can cause a b-integrin-related developmental defect in siRNA in HeLa cells suggested that VIP36 may also function as an ER export receptor [11]. * Corresponding author. Tel.: þ1 334 844 8727; fax: þ1 334 844 9208. It is now apparent that ERGIC-53 and VIP36 share similar L-type E-mail address: [email protected] (Z. Liu). lectin domains and mannose-binding selectivity but have distinct 1050-4648/$ e see front matter Ó 2011 Elsevier Ltd. All rights reserved. doi:10.1016/j.fsi.2011.12.009 H. Zhang et al. / Fish & Shellfish Immunology 32 (2012) 598e608 599 functions within the early secretory pathway [5]. Selective protein [32]. The signal peptides and conserved domains were searched by transport and sorting in the secretory pathway is fundamentally SMART program (http://smart.embl-heidelberg.de/). important for both healthy and diseased organisms. Within plant innate immune systems L-type lectins have been hypothesized to play a role as pattern recognition receptors while recent work in 2.2. Phylogenetic analysis mammalian systems indicates potential roles in infectious responses and phagocytosis [12e14]. Amino acid sequences of the LMAN, ERGIC-53 and VIP36 genes Although sequences of L-type lectins from teleost fish can be from various species were downloaded from NCBI and Ensembl identified in public gene databases, they have not been character- Genome Browser. A phylogenetic tree was constructed using the ized previously or examined for potential roles in immune neighbor-joining method within the Molecular Evolutionary responses. In channel catfish (Ictalurus punctatus), the primary Genetics Analysis (MEGA 4) package [33]. aquaculture species in the United States [15], a large number of genes involved in innate immunity have been characterized including antimicrobial peptides [16e18], Toll-like receptors [19], 2.3. Tissue sampling and RNA extraction NOD-like receptors [20], and a large number of chemokines, cyto- kines, and acute phase response proteins [21e25]. Additionally, we To determine gene expression in various healthy tissues, have previously characterized several other groups of lectins from samples of 11 tissues including brain, gill, heart, head-kidney, catfish including a C-type mannose-binding lectin [26]. However, trunk-kidney, intestine, liver, muscle, skin, spleen, and stomach no information is known about the nature of the L-type lectins and were collected. Due to small sample size of each individual fish, we their relationship with the immune response. Catfish production collected samples into three pools with tissues from 15 fish in each suffers heavy losses due to enteric septicemia of catfish (ESC), pool. The tissues were flash-frozen in liquid nitrogen and stored in caused by a Gram-negative intracellular bacterium Edwardsiella a À80 C ultrafreezer until RNA preparation. Tissues were homog- ictaluri [27]. ESC in its acute form is characterized by gastroenteric enized under liquid nitrogen using the RNeasy Plus Mini Kit (Qia- septicemia and, under artificial challenge, often results in heavy gen, Valencia, CA, USA) to extract total RNA following the mortalities as early as four days after onset of infection [28,29].To manufacturer’s instructions. First-strand cDNA was synthesized better understand the crucial innate immune response of channel using an iScript cDNA Synthesis Kit (Bio-Rad, USA) following the catfish in the context of ESC, and the possible involvement of L-type manufacturer’s instructions. lectins in the innate immune system of channel catfish, here we characterized three L-type lectins, conducted phylogenetic analysis, and analyzed their expression after ESC challenge. 2.4. Southern blot analysis 2. Materials and methods To determine the genomic copy number of L-type lectin genes in channel catfish, Southern blot analysis was conducted as previously fl m 2.1. Identification and sequencing of catfish L-type lectin cDNAs described [26]. Brie y, 10 g of genomic DNA isolated from each of three individual adult channel catfish was digested with 30 units of Based on the cDNA sequences of L-type lectin from zebrafish, we the restriction endonucleases EcoRI,Hind III or Pst I (New England m searched the channel catfish expressed sequence tags (ESTs) data- Biolabs, Beverly, MA) in a 25 L reaction at 37 C. The digested DNA base [30,31] in NCBI using BLAST. The clone CBPN21042 (GenBank samples were electrophoresed on a 0.8% agarose gel. After elec- ID: FD339357.1 and FD339356.1), CBPN25640 (GenBank ID: trophoresis, the gel was submerged in 0.25 N HCl for 15 min, then in FD345714.1 and FD345715.1) and CBPO11108 (GenBank ID: denaturation and neutralization buffer for 30 min, respectively. The FD041401.1 and FD041402.1) were determined to encode the DNA was transferred to an Immobilon positively-charged nylon putative complete cDNAs of catfish ERGIC-53, VIP36, and VIP36-like membrane (Millipore, Bedford, MA) by capillary transfer for 18 h  fi genes. These clones were re-sequenced to confirm the sequences using 20 SSC buffer. The DNA was xed to the membrane using using T7 and SP6 primers (Table 1), using the BigDye Terminator a UV cross-linker (Stratagene, La Jolla, CA) with the auto-crosslink v3.1 Cycle Sequencing kit (Applied Biosystems, Foster City, CA, USA) settings. The membrane was hybridized with cDNA probes ampli- fied using primers listed in Table 1. After pre-hybridization for 2 h with salmon sperm DNA and hybridization with a 32P-dCTP labeled Table 1 probe at 63 C for 16 h, the membrane was washed twice with wash Primers used in this study.
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